ID A0A3P8YYE6_ESOLU Unreviewed; 567 AA.
AC A0A3P8YYE6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Calcitonin receptor {ECO:0000256|ARBA:ARBA00017333};
GN Name=CALCR {ECO:0000313|Ensembl:ENSELUP00000021193.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000021193.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000021193.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000021193.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: Interacts with GPRASP2. {ECO:0000256|ARBA:ARBA00011681}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000256|ARBA:ARBA00005314}.
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DR AlphaFoldDB; A0A3P8YYE6; -.
DR STRING; 8010.ENSELUP00000021193; -.
DR Ensembl; ENSELUT00000041744.2; ENSELUP00000021193.2; ENSELUG00000020617.2.
DR GeneTree; ENSGT00940000155380; -.
DR InParanoid; A0A3P8YYE6; -.
DR OMA; PTTEAMW; -.
DR Proteomes; UP000265140; LG10.
DR Bgee; ENSELUG00000020617; Expressed in brain and 4 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:UniProt.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd15274; 7tmB1_calcitonin_R; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR001688; GPCR_2_calcitonin_rcpt.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF8; CALCITONIN RECEPTOR; 1.
DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 2.
DR PRINTS; PR00361; CALCITONINR.
DR PRINTS; PR01350; CTRFAMILY.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 2.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 2.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 2.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 243..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..101
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 150..234
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 244..491
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 567 AA; 65234 MW; 2E129D4530228BCB CRC64;
PPLEGVSDTA LGTSSKKCGR LPWWQMGPSR VLLKVFLPDA GAFCSRMWDG LLCWDETPVG
SYATQSCPGH HGVDTSGKVS KYCDESGNWV QSPSINTTWS NLPGFVWNRK CFSKYLVEPA
SLVPTLEIPF SPRVNQDEET RKKIIDSQYK CFEKMNRDLP YNKSGLYCNR TWDGWLCWED
TPAGTVSWQN CPNYFQDFDS TEKATKICTE SGQWFRHPDT NRTWSNYTLC NYHTTGKLKM
AYILYYMAIV GHALSIASLM ISLAIFFYFR SLSCQRITLH KNLFVSYVLN SALTLIYLIA
VVNNPDVVER NPVGCKVLHF FHMYMLGCNY FWMLCEGIYL HTLIVVAVFA EEQRLHWYYL
LGWGFPLVPA SIHAVARKKY FDDNCWMSVE THLLYVVHGP IMAALLVNLF FLLNIVRVLV
TKLRDTHRAE SNMYMKAVRA TLILVPLLGI QFVIFPWRPE NRLVGEIYDY IMHILMHYQG
LLVATIFCFF NGEVQAALKR QWVQYKAQWG QRRRDHCSMR STSYTATSIT EVPSFMYHHD
CSSEHLNGRH AADQSELVAL KSADACA
//
